| S-6-hydroxynicotine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.3.5 | ||||||||
| CAS no. | 37256-29-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a (S)-6-hydroxynicotine oxidase ( EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction
- (S)-6-hydroxynicotine + H2O + O2 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
The 3 substrates of this enzyme are (S)-6-hydroxynicotine, H2O, and O2, whereas its two products are 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is (S)-6-hydroxynicotine:oxygen oxidoreductase. Other names in common use include L-6-hydroxynicotine oxidase, 6-hydroxy-L-nicotine oxidase, and 6-hydroxy-L-nicotine:oxygen oxidoreductase. It employs one cofactor, FAD.
References
- Dai VD, Decker K, Sund H (1968). "Purification and properties of L-6-hydroxynicotine oxidase". Eur. J. Biochem. 4 (1): 95–102. doi: 10.1111/j.1432-1033.1968.tb00177.x. PMID 5646150.
- Decker K, Bleeg H (1965). "Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans". Biochim. Biophys. Acta. 105 (2): 313–24. doi: 10.1016/s0926-6593(65)80155-2. PMID 5849820.
